Journal
CATALYSTS
Volume 11, Issue 4, Pages -Publisher
MDPI
DOI: 10.3390/catal11040520
Keywords
enzyme immobilization; transaminase; amino acid dehydrogenase; flow biocatalysis
Categories
Funding
- Biotechnology and Biological Research Council [BB/P002536/1]
- Biotechnology and Biological Sciences Research Council [BB/R021287/1, 61]
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Transaminases are important biocatalysts for amine production, but their stability remains a concern. Recycling systems for the amino donor can help push unfavourable equilibrium reactions and reduce the need for high amino donor concentrations.
Transaminases have arisen as one of the main biocatalysts for amine production but despite their many advantages, their stability is still a concern for widespread application. One of the reasons for their instability is the need to use an excess of the amino donor when trying to synthesise amines with unfavourable equilibria. To circumvent this, recycling systems for the amino donor, such as amino acid dehydrogenases or aldolases, have proved useful to push the equilibria while avoiding high amino donor concentrations. In this work, we report the use of a new alanine dehydrogenase from the halotolerant bacteria Halomonas elongata which exhibits excellent stability to different cosolvents, combined with the well characterised CbFDH as a recycling system of L-alanine for the amination of three model substrates with unfavourable equilibria. In a step forward, the amino donor recycling system has been co-immobilised and used in flow with success as well as re-used as a dialysis enclosed system for the amination of an aromatic aldehyde.
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